Copper proteins are immensely important in biological processes, yet relatively little firm knowledge exists concerning the structure of the protein copper environment. We propose to study the binding of copper in proteins (identity of bound residues and their geometry) using resonance Raman spectroscopy and, secondarily, infrared circular dichroism. Coppersulfur and Copper (III) complexes will also be studied, to extend knowledge of vibrational frequencies in simple species, for comparison to the proteins. The general method will be to employ the resonance Raman technique to provide vibrational (and therefore structural) information on a specific protein chromophore. Since the various types of protein-bound copper have distinct chromophoric properties, it will be possible to observe Raman spectra of each type of copper independently of the others, even in complex, multicopper systems. We propose to use the resonance Raman, vibrational, and electronic spectral information which we develop for simple systems, together with existing data, to elucidate the structures of various types of copper ("blue" copper, paired copper, etc.) in simple proteins. This will in turn form the background for structural interpretation of the resonance Raman spectra of the multicopper oxidases. The structural information thus gained will be related to the functional characteristics of protein-bound copper. The objectives of the study are to elucidate the roles of copper in normal and pathological metabolism, and to provide a detailed basis for understanding pathological conditions of copper metabolism and copper-dependent metabolism, such as the debilitating Wilson's disease and the fatal Menkes' kinky hair syndrome.